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Thakur, Naveen; Ray, Arka P; Sharp, Liam; Jin, Beining; Duong, Alexander; Pour, Niloofar Gopal; Obeng, Samuel; Wijesekara, Anuradha V; Gao, Zhan-Guo; McCurdy, Christopher R; Jacobson, Kenneth A; Lyman, Edward; Eddy, Matthew T
Nature communications, 02/2023, Letnik: 14, Številka: 1Journal Article
G protein-coupled receptors (GPCRs) are embedded in phospholipids that strongly influence drug-stimulated signaling. Anionic lipids are particularly important for GPCR signaling complex formation, but a mechanism for this role is not understood. Using NMR spectroscopy, we explore the impact of anionic lipids on the function-related conformational equilibria of the human A adenosine receptor (A AR) in bilayers containing defined mixtures of zwitterionic and anionic phospholipids. Anionic lipids prime the receptor to form complexes with G proteins through a conformational selection process. Without anionic lipids, signaling complex formation proceeds through a less favorable induced fit mechanism. In computational models, anionic lipids mimic interactions between a G protein and positively charged residues in A AR at the receptor intracellular surface, stabilizing a pre-activated receptor conformation. Replacing these residues strikingly alters the receptor response to anionic lipids in experiments. High sequence conservation of the same residues among all GPCRs supports a general role for lipid-receptor charge complementarity in signaling.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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